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Science 23 December 1988:
Vol. 242. no. 4886, pp. 1678 - 1681
DOI: 10.1126/science.2849208
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Articles

Science, Vol 242, Issue 4886, 1678-1681
Copyright © 1988 by American Association for the Advancement of Science

articles

Restoration of torque in defective flagellar motors

DF Blair and HC Berg

Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.

Paralyzed motors of motA and motB point and deletion mutants of Escherichia coli were repaired by synthesis of wild-type protein. As found earlier with a point mutant of motB, torque was restored in a series of equally spaced steps. The size of the steps was the same for both MotA and MotB. Motors with one torque generator spent more time spinning counterclockwise than did motors with two or more generators. In deletion mutants, stepwise decreases in torque, rare in point mutants, were common. Several cells stopped accelerating after eight steps, suggesting that the maximum complement of torque generators is eight. Each generator appears to contain both MotA and MotB.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Mutational Analysis of the Flagellar Protein FliG: Sites of Interaction with FliM and Implications for Organization of the Switch Complex.
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How 34 Pegs Fit into 26 + 8 Holes in the Flagellar Motor.
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Cysteine-Scanning Mutagenesis of the Periplasmic Loop Regions of PomA, a Putative Channel Component of the Sodium-Driven Flagellar Motor in Vibrio alginolyticus.
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D. R. Thomas, D. G. Morgan, and D. J. DeRosier (1999)
PNAS 96, 10134-10139
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Flagellar determinants of bacterial sensitivity to chi -phage.
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Function of Proline Residues of MotA in Torque Generation by the Flagellar Motor of Escherichia coli.
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Stepped versus continuous rotatory motors at the molecular scale.
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Intermolecular Cross-linking between the Periplasmic Loop3-4 Regions of PomA, a Component of the Na+-driven Flagellar Motor of Vibrio alginolyticus.
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